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News

Making proteins glow blue

Fraunhofer-Gesellschaft Zur Forderung Der Angewandten Forschung E.V. : 30 September, 2003  (New Product)
In the beginning, there was protein. 19th-century scientists at least believed that this group of organic compounds were based on some kind of primeval matter. Therefore they named them 'proteins', derived from the Greek word 'protos' (the first). It is meanwhile known that the structure of proteins is ultimately determined by the genome.
In the beginning, there was protein. 19th-century scientists at least believed that this group of organic compounds were based on some kind of primeval matter. Therefore they named them 'proteins', derived from the Greek word 'protos' (the first). It is meanwhile known that the structure of proteins is ultimately determined by the genome. From a functional point of view, this wide variety of molecules in all living organisms comes after the DNA. Proteome research, which has developed rapidly since the nearly complete decoding of the human ge-nome, involves numerous automated processes. In the fields of pharmaceuticals, medicine, environmental analysis and biotechnology, large quantities of various proteins are often screened to determine their action mechanisms. Another vital question is: How is this related to the protein's molecular structure?

The commoner analysis techniques rely on the fact that a known biomolecule fixed to a chip binds only with one specific protein. This complex formation is then revealed through an automated optical screening device by staining them with chemical dyes. A major disadvantage of this method is that the dyes change the structure and thereby the function of the proteins. The Fraunhofer Alliance for Protein Chips, in which seven institutes have participated over the past year, introduces a new screening device that eliminates this disadvantage. It can be seen at the BioTechnica trade show in Hanover, October 7-9 (Hall 3, Stand F 24).

'This still one-of-a-kind device takes advantage of the fact that most proteins are naturally fluorescent', explains Dr. Christian Hoffmann, responsible for marketing at the Fraunhofer Institute for Physical Measurement Techniques IPM. 'We use tryptophan, an amino acid found in almost all proteins. A 300-watt arc lamp stimulates the proteins in the near ultraviolet range. It reacts by emitting blue fluorescent light at a wavelength of 340 nanometers.' The resulting pattern of bright dots is recorded with an electronic camera, enabling laboratory technicians to quickly compare the fluorescence pattern with that of the protein chip. The lab can now identify the sample in which a reaction has occurred, for instance between a receptor and a ligand. But the biochemist generally wants more than a simple and qualitative 'yes / no' answer. To provide a quantitative analysis, the device measures the intensity of the fluorescent light. This allows the concentration to be calculated, as the researchers have already proven using model proteins.
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